All Publications

  • The Mechanism and Function of Group II Chaperonins. Journal of molecular biology Lopez, T., Dalton, K., Frydman, J. 2015; 427 (18): 2919-2930


    Protein folding in the cell requires the assistance of enzymes collectively called chaperones. Among these, the chaperonins are 1-MDa ring-shaped oligomeric complexes that bind unfolded polypeptides and promote their folding within an isolated chamber in an ATP-dependent manner. Group II chaperonins, found in archaea and eukaryotes, contain a built-in lid that opens and closes over the central chamber. In eukaryotes, the chaperonin TRiC/CCT is hetero-oligomeric, consisting of two stacked rings of eight paralogous subunits each. TRiC facilitates folding of approximately 10% of the eukaryotic proteome, including many cytoskeletal components and cell cycle regulators. Folding of many cellular substrates of TRiC cannot be assisted by any other chaperone. A complete structural and mechanistic understanding of this highly conserved and essential chaperonin remains elusive. However, recent work is beginning to shed light on key aspects of chaperonin function and how their unique properties underlie their contribution to maintaining cellular proteostasis.

    View details for DOI 10.1016/j.jmb.2015.04.013

    View details for PubMedID 25936650

  • The Dynamic Conformational Cycle of the Group I Chaperonin C-Termini Revealed via Molecular Dynamics Simulation PLOS ONE Dalton, K. M., Frydman, J., Pande, V. S. 2015; 10 (3)

    View details for DOI 10.1371/journal.pone.0117724

    View details for Web of Science ID 000352134700014

    View details for PubMedID 25822285